ZN131_HUMAN
ID ZN131_HUMAN Reviewed; 623 AA.
AC P52739; B4DRL3; Q6PIF0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger protein 131;
GN Name=ZNF131;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-589 (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-623 (ISOFORM 1).
RC TISSUE=Insulinoma;
RX PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA Tommerup N., Vissing H.;
RT "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs
RT identify putative candidate genes for developmental and malignant
RT disorders.";
RL Genomics 27:259-264(1995).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12163020; DOI=10.1016/s0006-291x(02)00850-1;
RA Trappe R., Buddenberg P., Uedelhoven J., Glaser B., Buck A., Engel W.,
RA Burfeind P.;
RT "The murine BTB/POZ zinc finger gene Znf131: predominant expression in the
RT developing central nervous system, in adult brain, testis, and thymus.";
RL Biochem. Biophys. Res. Commun. 296:319-327(2002).
RN [7]
RP NUCLEAR LOCALIZATION SIGNALS, AND SUBCELLULAR LOCATION.
RX PubMed=17306895; DOI=10.1016/j.bbamcr.2006.12.005;
RA Donaldson N.S., Daniel Y., Kelly K.F., Graham M., Daniel J.M.;
RT "Nuclear trafficking of the POZ-ZF protein Znf131.";
RL Biochim. Biophys. Acta 1773:546-555(2007).
RN [8]
RP FUNCTION.
RX PubMed=18847501; DOI=10.1186/1471-2164-9-476;
RA Han X., Guo J., Deng W., Zhang C., Du P., Shi T., Ma D.;
RT "High-throughput cell-based screening reveals a role for ZNF131 as a
RT repressor of ERalpha signaling.";
RL BMC Genomics 9:476-476(2008).
RN [9]
RP FUNCTION, UBIQUITINATION, SUMOYLATION AT LYS-601, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-242; LYS-281; LYS-289; LYS-477; LYS-601 AND LYS-610.
RX PubMed=22467880; DOI=10.1074/jbc.m111.336354;
RA Oh Y., Chung K.C.;
RT "Small ubiquitin-like modifier (SUMO) modification of zinc finger protein
RT 131 potentiates its negative effect on estrogen signaling.";
RL J. Biol. Chem. 287:17517-17529(2012).
RN [10]
RP UBIQUITINATION, SUMOYLATION AT LYS-601, AND SUBCELLULAR LOCATION.
RX PubMed=23404503; DOI=10.1074/jbc.m112.438234;
RA Oh Y., Chung K.C.;
RT "UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3
RT ligase for zinc finger protein 131.";
RL J. Biol. Chem. 288:9102-9111(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-289 AND LYS-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Plays a role during development and organogenesis as well as
CC in the function of the adult central nervous system (By similarity).
CC May be involved in transcriptional regulation as a repressor of
CC ESR1/ER-alpha signaling. {ECO:0000250, ECO:0000269|PubMed:18847501,
CC ECO:0000269|PubMed:22467880}.
CC -!- INTERACTION:
CC P52739-2; Q14192: FHL2; NbExp=6; IntAct=EBI-10213055, EBI-701903;
CC P52739-2; Q5TD97: FHL5; NbExp=4; IntAct=EBI-10213055, EBI-750641;
CC P52739-2; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-10213055, EBI-10269566;
CC P52739-2; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-10213055, EBI-11532361;
CC P52739-2; P40337-2: VHL; NbExp=3; IntAct=EBI-10213055, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17306895,
CC ECO:0000269|PubMed:22467880, ECO:0000269|PubMed:23404503}.
CC Note=Sumoylation does not affect nuclear localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52739-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52739-2; Sequence=VSP_016923;
CC -!- TISSUE SPECIFICITY: Predominant expression is found in different brain
CC areas such as the occipital and temporal lobe, the nucleus caudatus,
CC hippocampus, and the cerebellum as well as in testis and thymus.
CC {ECO:0000269|PubMed:12163020}.
CC -!- PTM: Monosumoylated at Lys-601 by CBX4 and UHRF2. Sumoylation may
CC potentiate ZNF131 inhibition of estrogen signaling. Sumoylation does
CC not interfere with ubiquitination. {ECO:0000269|PubMed:22467880,
CC ECO:0000269|PubMed:23404503}.
CC -!- PTM: Ubiquitinated.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK057343; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK299315; BAG61325.1; -; mRNA.
DR EMBL; AC106800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471119; EAW56046.1; -; Genomic_DNA.
DR EMBL; BC035875; AAH35875.1; -; mRNA.
DR EMBL; U09410; AAC50251.1; -; mRNA.
DR CCDS; CCDS43313.1; -. [P52739-2]
DR CCDS; CCDS78005.1; -. [P52739-1]
DR PIR; I38597; I38597.
DR RefSeq; NP_001284477.1; NM_001297548.2. [P52739-1]
DR RefSeq; NP_001317636.1; NM_001330707.1. [P52739-1]
DR RefSeq; NP_001317637.1; NM_001330708.1. [P52739-1]
DR RefSeq; NP_001317641.1; NM_001330712.1. [P52739-1]
DR RefSeq; NP_001317643.1; NM_001330714.1. [P52739-1]
DR RefSeq; NP_001317646.1; NM_001330717.1.
DR RefSeq; XP_005248420.1; XM_005248363.4.
DR RefSeq; XP_016865319.1; XM_017009830.1.
DR RefSeq; XP_016865327.1; XM_017009838.1.
DR AlphaFoldDB; P52739; -.
DR SMR; P52739; -.
DR BioGRID; 113485; 118.
DR IntAct; P52739; 32.
DR MINT; P52739; -.
DR STRING; 9606.ENSP00000421246; -.
DR iPTMnet; P52739; -.
DR PhosphoSitePlus; P52739; -.
DR BioMuta; ZNF131; -.
DR DMDM; 85681857; -.
DR EPD; P52739; -.
DR jPOST; P52739; -.
DR MassIVE; P52739; -.
DR MaxQB; P52739; -.
DR PeptideAtlas; P52739; -.
DR PRIDE; P52739; -.
DR ProteomicsDB; 56512; -. [P52739-1]
DR ProteomicsDB; 56513; -. [P52739-2]
DR Antibodypedia; 23236; 280 antibodies from 23 providers.
DR DNASU; 7690; -.
DR Ensembl; ENST00000306938.8; ENSP00000305804.4; ENSG00000172262.12. [P52739-2]
DR Ensembl; ENST00000505606.6; ENSP00000423945.1; ENSG00000172262.12. [P52739-2]
DR Ensembl; ENST00000509156.5; ENSP00000426504.1; ENSG00000172262.12. [P52739-1]
DR Ensembl; ENST00000509634.5; ENSP00000421246.1; ENSG00000172262.12. [P52739-2]
DR Ensembl; ENST00000682664.1; ENSP00000507111.1; ENSG00000172262.12. [P52739-1]
DR GeneID; 7690; -.
DR KEGG; hsa:7690; -.
DR MANE-Select; ENST00000682664.1; ENSP00000507111.1; NM_001330707.2; NP_001317636.1.
DR UCSC; uc003jnk.4; human. [P52739-1]
DR CTD; 7690; -.
DR DisGeNET; 7690; -.
DR GeneCards; ZNF131; -.
DR HGNC; HGNC:12915; ZNF131.
DR HPA; ENSG00000172262; Low tissue specificity.
DR MIM; 604073; gene.
DR neXtProt; NX_P52739; -.
DR OpenTargets; ENSG00000172262; -.
DR PharmGKB; PA37504; -.
DR VEuPathDB; HostDB:ENSG00000172262; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154668; -.
DR HOGENOM; CLU_031851_0_0_1; -.
DR InParanoid; P52739; -.
DR OMA; KEHLMCH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P52739; -.
DR TreeFam; TF331428; -.
DR PathwayCommons; P52739; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR SignaLink; P52739; -.
DR BioGRID-ORCS; 7690; 705 hits in 1151 CRISPR screens.
DR ChiTaRS; ZNF131; human.
DR GenomeRNAi; 7690; -.
DR Pharos; P52739; Tbio.
DR PRO; PR:P52739; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P52739; protein.
DR Bgee; ENSG00000172262; Expressed in secondary oocyte and 199 other tissues.
DR ExpressionAtlas; P52739; baseline and differential.
DR Genevisible; P52739; HS.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR027758; Zfp131.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24399:SF35; PTHR24399:SF35; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..623
FT /note="Zinc finger protein 131"
FT /id="PRO_0000047413"
FT DOMAIN 34..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 261..283
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..311
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..381
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 420..443
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 573..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..148
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000269|PubMed:17306895"
FT MOTIF 317..328
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000269|PubMed:17306895"
FT COMPBIAS 573..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 244..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016923"
FT MUTAGEN 242
FT /note="K->R: No effect on sumoylation; when associated with
FT R-281 and R-289."
FT /evidence="ECO:0000269|PubMed:22467880"
FT MUTAGEN 281
FT /note="K->R: No effect on sumoylation; when associated with
FT R-242 and R-281."
FT /evidence="ECO:0000269|PubMed:22467880"
FT MUTAGEN 289
FT /note="K->R: No effect on sumoylation; when associated with
FT R-242 and R-281."
FT /evidence="ECO:0000269|PubMed:22467880"
FT MUTAGEN 477
FT /note="K->R: Small loss of sumoylation. Complete loss of
FT CBX4 sumoylation; when associated with R-601 and R-610."
FT /evidence="ECO:0000269|PubMed:22467880"
FT MUTAGEN 601
FT /note="K->R: Significant loss of sumoylation. Complete loss
FT of CBX4 sumoylation; when associated with R-477 and R-610."
FT /evidence="ECO:0000269|PubMed:22467880"
FT MUTAGEN 610
FT /note="K->R: No effect on sumoylation. Complete loss of
FT CBX4 sumoylation; when associated with R-477 and R-601."
FT /evidence="ECO:0000269|PubMed:22467880"
FT CONFLICT 148..151
FT /note="AETS -> CSKA (in Ref. 5; AAC50251)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="GT -> A (in Ref. 5; AAC50251)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="H -> R (in Ref. 1; AK057343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 71422 MW; E2720D922A39572C CRC64;
MEAEETMECL QEFPEHHKMI LDRLNEQREQ DRFTDITLIV DGHHFKAHKA VLAACSKFFY
KFFQEFTQEP LVEIEGVSKM AFRHLIEFTY TAKLMIQGEE EANDVWKAAE FLQMLEAIKA
LEVRNKENSA PLEENTTGKN EAKKRKIAET SNVITESLPS AESEPVEIEV EIAEGTIEVE
DEGIETLEEV ASAKQSVKYI QSTGSSDDSA LALLADITSK YRQGDRKGQI KEDGCPSDPT
SKQVEGIEIV ELQLSHVKDL FHCEKCNRSF KLFYHFKEHM KSHSTESFKC EICNKRYLRE
SAWKQHLNCY HLEEGGVSKK QRTGKKIHVC QYCEKQFDHF GHFKEHLRKH TGEKPFECPN
CHERFARNST LKCHLTACQT GVGAKKGRKK LYECQVCNSV FNSWDQFKDH LVIHTGDKPN
HCTLCDLWFM QGNELRRHLS DAHNISERLV TEEVLSVETR VQTEPVTSMT IIEQVGKVHV
LPLLQVQVDS AQVTVEQVHP DLLQDSQVHD SHMSELPEQV QVSYLEVGRI QTEEGTEVHV
EELHVERVNQ MPVEVQTELL EADLDHVTPE IMNQEERESS QADAAEAARE DHEDAEDLET
KPTVDSEAEK AENEDRTALP VLE
